Analytical Data
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基因名
TRIM62
- Application
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别名
6330414G21Rik; AI450348; DEAR1; ductal epithelium-associated RING Chromosome 1; E3 ubiquitin-Protein ligase TRIM62; FLJ10759; FLJ16558 ; MGC115263; TRI62_HUMAN; TRIM62; Tripartite motif containing 62; Tripartite motif-containing Protein 62
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9BVG3
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表达区间
1-475 aa
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氨基酸序列
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC PECRRTFAEP ALAPSLKLAN IVERYSSFPL DAILNARRAA RPCQAHDKVK LFCLTDRALL CFFCDEPALH EQHQVTGIDD AFDELQRELK DQLQALQDSE REHTEALQLL KRQLAETKSS TKSLRTTIGE AFERLHRLLR ERQKAMLEEL EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD RHTFLAGVAS LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTLD PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV HYWEVVVAEK TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC TEPWTRLNVR DKLDKVGVFL DYDQGLLIFY NADDMSWLYT FREKFPGKLC SYFSPGQSHA NGKNVQPLRI NTVRI
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分子量
54.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TRIM62, a member of the tripartite motif (TRIM) family of proteins, has garnered attention in recent years due to its potential roles in various cellular processes, including immune response, cell proliferation, and apoptosis. This protein features an RING domain, two B-box motifs, and a coiled-coil domain, which are characteristic of TRIM proteins, enabling it to function in protein-protein interactions and ubiquitination processes. Studies have suggested that TRIM62 may play a crucial role in modulating the immune response by influencing the signaling pathways associated with inflammation and viral infections. Furthermore, research has indicated that TRIM62 could be involved in tumorigenesis and cancer progression, potentially serving as a biomarker or therapeutic target in certain malignancies. Given its diverse functions and implications in health and disease, the recombinant expression of TRIM62 is essential for elucidating its molecular mechanisms and interactions. The generation of TRIM62 recombinant protein allows for detailed biochemical assays, structural studies, and the exploration of its functional roles within cell models. This research ultimately aims to clarify TRIM62’s contributions to cellular homeostasis and its potential as a target for novel therapeutic strategies in disease management.
